Abstract
Immunoglobulins (Ig’s) are polyfunctional molecules. The most thoroughly studied, and currently best understood, of the numerous functions of this protein family is antigen-binding, a subject that is discussed in detail in several other chapters of this volume. The various other functions are collectively referred to as the biological properties, or effector functions, of antibodies. These properties are mediated by the constant (C) regions of the heavy (H) chains of the various Ig molecules. In fact, most of the properties recognized at present have been associated with that carboxyterminal subcomponent of the H-chain C region referred to as the Fc (constant) segment, or fragment.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Allen, J. C., and Kunkel, H. G., 1966, Hidden rheumatoid factors with specificity for native y globulins, Arthritis Rheum. 9:758–768.
Basten, A., Miller, J. F. A. P., Sprent, J., and Prize, J., 1972, A receptor for antibody on B lymphocytes. I. Method of detection and functional significance, J. Exp. Med. 135:610–626.
Bennich, H., and von Bahr-Lindstrom, H., 1974, Structure of immunoglobulin E (IgE), Prog. Immunol. II 1:49–58.
Bennich, H., Ishizaka, K., Ishizaka, T., and Johansson, S. G. 0., 1969, Immunoglobulin E: A comparative antigenic study of yE globulin and myeloma IgND, J. Immunol. 102:826–831.
Berken, A., and Benacerraf, B., 1966, Properties of antibodies cytophilic for macrophages, J. Exp. Med. 123:119–144.
Brambell, F. W. R., 1966, The transmission of immunity from mother to young and the catabolism of immunoglobulins, Lancet 2:1087–1088.
Brambell, F. W. R., 1970, in: The Transmission of Passive Immunity from Mother to Young (A. Neuberger and E. L. Tatum, eds.), pp. North-Holland, Amsterdam and London.
Brambell, F. W. R., Hemmings, W. A., Oakley, C. L., and Porter, R. R., 1960, Relative transmission of the fractions of papain hydrolyzed homologous y-globulin from the uterine cavity to the foetal circulation in the rabbit, Proc. R. Soc. London Ser. B 151:478–482.
Brown, J. C., and Koshland, M. E., 1975, Activation of antibody Fc function by antigen-induced conformational changes, Proc. Natl. Acad. Sci. U.S.A. 72:5111–5115.
Capra, J. D., and Kehoe, J. M., 1974, Structure of antibodies with shared idiotypy: The complete sequence of the heavy chain variable regions of two immunoglobulin M anti-gamma globulins, Proc. Natl. Acad. Sci. U.S.A. 71:4032–4036.
Capra, J. D., Kehoe, J. M., Winchester, R. J., and Kunkel, H. G., 1971, Structure—function relationships among anti-gamma globulin antibodies, Ann. N.Y. Acad. Sci. 190:371–381.
Carson, D., Kulczycki, A., Jr., and Metzger, H., 1975, Interaction of IgE with rat basophilic leukemic cells. IV. Release of intact receptors on cell-free particles, J. Immunol. 114:158–160.
Ciccimarra, F., Rosen, F. S., and Menler, E., 1975, Localization of the IgG effector site for monocyte receptors, Proc. Natl. Acad. Sci. U.S.A. 72:2081–2086.
Colomb, M., and Porter, R. R., 1975, Characterization of a plasmin-digest fragment of rabbit immunoglobulin gamma that binds antigen and complement, Biochem. J. 145:177–183.
Connell, G. E., and Porter, R. R., 1971, A new enzymic fragment (Fach) of rabbit immunoglobulin G, Biochem. J. 124:53p.
Cresswell, P., Springer, T., Strominger, J. L., Turner, M. J., Grey, H. M., and Kubo, R. T., 1974, Immunological identity of the small subunit of HLA antigens and beta 2 microglobulin and its turnover on the cell membrane, Proc. Natl. Acad. Sci. U.S.A. 71:2123–2127.
Cunningham, B. A., Wang, J. L., Berggârd, I., and Peterson, P. A., 1973, The complete amino acid sequence of ß 2 microglobulin, Biochemistry 12:4811–4822.
Deisenhofer, J., Colman, P. M., Epp, O., and Huber, R., 1976, Crystallographic structural studies of a human Fc fragment. II. A complete model based on a Fourier map at 3.5 A resolution, HoppeSeyler’s Z. Physiol. Chem. 357: 1421–1434.
Dickler, H. B., and Kunkel, H. G., 1972, Interaction of aggregated y globulin with B lymphocytes, J. Exp. Med. 136:191–196.
Dorrington, K. J., and Bennich, H., 1973, Thermally induced structural changes in immunoglobulin E, J. Biol. Chem. 248:8378–8384.
Dorrington, K. J., and Painter, R. H., 1974, Functional domains of immunoglobulin G, Prog. Immunol. II 1:75–84.
Dorval, G., Welsh, K. I., and Wigzell, H., 1974, Labelled staphylococcal protein A as an immunological probe in the analysis of cell surface markers, Scand. J. Immunol. 3:405–411.
Edelman, G. M., 1970, The covalent structure of a human yG-immunoglobulin. XI. Functional implications, Biochemistry 9:3197–3205.
Edelman, G. M., Cunningham, B. A., Gall, W. E., Gottlieb, P. D., Rutishauser, U., and Waxdal, M. J., 1969, The covalent structure of an entire yG immunoglobulin molecule, Proc. Natl. Acad. Sci. U.S.A. 63:78–85.
Eisen, H. N., 1974, Immunology, p. 483, Harper and Row, Hagerstown, Maryland.
Ellerson, J. R., Yasmeen, D., Painter, R. H., and Dorrington, K. J., 1972, A fragment corresponding to the CH2 region of immunoglobulin G (IgG) with complement fixing activity, FEBS Lett. 24:318–322.
Fireman, P., Vannier, W. E., and Goodman, H. C., 1963, The association of skin-sensitizing antibody with the N2a globulins in sera from ragweed sensitive patients, J. Exp. Med. 117:603–619.
Forsgren, A., and Nordström, K., 1974, Protein A of Staphylococcus aureus: The biological significance of its reaction with IgG, Ann. N.Y. Acad. Sci. 236:252–266.
Forsgren, A., and Sjoquist, J., 1966, Protein A from S. aureus. I. Pseudo-immune reaction with human y-globulin, J. Immunol. 99:822–827.
Gaarder, P. I., and Natvig, J. B., 1970, Hidden rheumatoid factors reacting with “Non a” and other antigens of native autologous IgG, J. Immunol. 105:928–937.
Good, R. A., and Day, N. K. (eds.), 1977, Comprehensive Immunology, Vol. 2, Biological Amplification Systems in Immunology,Plenum Press, New York.
Gotze, O., and Müller-Eberhard, H. J., 1971, The C3-activator system: An alternate pathway of complement activation, J. Exp. Med. 134:90s.
Grubb, R., 1970, The Genetic Markers of Human Immunoglobulins, Springer-Verlag, New York.
Guyer, R. L., Koshland, M. E., and Knopf, P. M., 1976, Immunoglobulin binding by mouse intestinal epithelial cell receptors, J. Immunol. 117:587–593.
Heremans, J. F., and Vaerman, J. P., 1962, ß2a-Globulin as a possible carrier of allergic reaginic activity, Nature (London) 193:1091–1092.
Huber, H., Douglas, S. D., Nusbacher, J., Kochwa, S., and Rosenfield, R. E., 1971, IgG subclass specificity of human monocyte receptor sites, Nature (London) 229:419–420.
Huber, R., Deisenhofer, J., Colman, P. M., Matsushima, M., and Palm, W., 1976, Crystallographic structure studies of an IgG molecule and an Fc fragment, Nature (London) 264:415–420.
Huber, R., Deisenhofer, J., Colman, P., Matsushima, M., and Palm, W., 1977, X-ray diffraction analysis of immunoglobulin structure, in: Mosbacher Kolloquium der Gesellschaft für Biologische Chimie: Das Immunsystem (F. Melchers and K. Rajewsky, eds.), pp. 26–40, Springer-Verlag, Berlin—Heidelberg—New York.
Hurst, M. M., Volanakis, J. E., Hester, R. B., Stroud, R. M., and Bennett, J. C., 1974, The structural basis for binding of complement by immunoglobulin M, J. Exp. Med. 140:1117–1121.
Hurst, M. M., Volanakis, J. E., Stroud, R. M., and Bennett, J. C., 1975, C1 fixation and classical complement pathway activation by a fragment of the Cµ4 domain of IgM, J. Exp. Med. 142:1322–1326.
Isenman, D. E., Dorrington, K. J., and Painter, R. H., 1975a, The structure and function of immunoglobulin domains. II. The importance of interchain disulfide bonds and the possible role of molecular flexibility in the interaction between immunoglobulin G and complement, J. Immunol. 114:1726–1729.
Isenman, D. E., Painter, R. H., and Dorrington, K. J., 1975b, The structure and function of immunoglobulin domains: Studies with beta-2-microglobulin on the role of the intrachain disulfide bond, Proc. Natl. Acad. Sci. U.S.A. 72:548–552.
Isenman, D. E., Ellerson, J. R., Painter, R. H., and Dorrington, K. J., 1977, Correlation between the exposure of aromatic chromophores at the surface of the Fc domains of immunoglobulin G and their ability to bind complement, Biochemistry 16:233–240.
Isersky, C., Mendoza, G., and Metzger, H., 1977, Reaction of antibodies with the cell surface receptor for IgE, Fed. Proc. Fed. Am. Soc. Exp. Biol. 36:12–17.
Ishizaka, K., and Ishizaka, T., 1968, Induction of erythema-wheal reactions by soluble antigen-yE antibody complexes in humans, J. Immunol. 101:68–78.
Ishizaka, K., and Ishizaka, T., 1971, IgE and reaginic hypersensitivity, Ann. N. Y. Acad. Sci. 190:443–456.
Ishizaka, K., Ishizaka, T., and Hornbrook, M. M., 1966, Physicochemical properties of human reaginic antibody. IV. Presence of a unique immunoglobulin as a carrier of reagmic activity, J. Immunol. 97:75–85.
Ishizaka, K., Ishizaka, T., and Lee, E. H., 1970a, Biologic function of the Fc fragments of E myeloma protein, Immunochemistry 7:687–702.
Ishizaka, K., Tomioka, H., and Ishizaka, T., 1970b, Mechanisms of passive sensitization. I. Presence of IgE and IgG molecules on human leukocytes, J. Immunol. 105:1459–1467.
Ishizaka, T., and Ishizaka, K., 1975, Biology of immunoglobulin E: Molecular basis of reaginic hypersensitivity, Prog. Allergy 19:60–121.
Ishizaka, T., Ishizaka, K., Salmon, S., and Fudenberg, H., 1967, Biologic activities of aggregated immunoglobulins of different classes, J. Immunol. 99:82–91.
Ishizaka, T., Sian, C. M., and Ishizaka, K., 1971, Complement fixation by aggregated IgE through the alternate pathway, J. Immunol. 108:848–851.
Ishizaka, T., Soto, C., and Ishizaka, K., 1973, Mechanisms of passive sensitization. III. Number of IgE molecules and its receptor sites on human basophil granulocytes, J. Immunol. 111:500–511.
Jensen, K., 1958, A noramlly occurring staphylococcus antibody in human serum, Acta Pathol. Microbiol. Scand. 44:421–428.
Johnson, B. J., and Thames, K. E., 1976, Investigations of the complement fixing sites of immunoglobulins, J. Immunol. 117:1491–1494.
Kehoe, J. M., Fougereau, M., and Bourgois, A., 1969, Immunoglobulin peptide with complement fixing activity, Nature (London) 224:1212–1213.
Kehoe, J. M., Bourgois, A., Capra, J. D., and Fougereau, M., 1974, Amino acid sequence of a murine immunoglobulin fragment that possesses complement fixing activity, Biochemistry 13:2499–2504.
Kronvall, G., and Frommel, D., 1970, Definition of staphylococcal protein A reactivity for human immunoglobulin G fragments, Immunochemistry 7:124–126.
Kronvall, G., and Williams, R. C., Jr., 1969, Differences in anti-protein A activity among IgG sub-groups, J. Immunol. 103:828–833.
Kronvall, G., Seal, U. S., Finstad, J., and Williams, R. C., Jr., 1970, Phylogenetic insight into evolution of mammalian Fc fragment of yG globulin using staphylococcal protein A, J. Immunol. 104:140–147.
Kulczycki, A., Jr., and Metzger, H., 1974, The interaction of IgE with rat basophilic leukemia cells. II. Quantitative aspects of the binding reaction, J. Exp. Med. 140:1676–1695.
Kunkel, H. G., Agnello, V., Joslin, F. G., Winchester, R. J., and Capra, J. D., 1973, Cross idiotypic specificity among monoclonal IgM proteins with anti-y-globulin activity, J. Exp. Med. 137:331–342.
Lancet, D., and Pecht, I., 1976, Kinetic evidence for hapten-induced conformational transition in immunoglobulin MOPC-460, Proc. Natl. Acad. Sci. U.S.A. 73:3549–3553.
Lawrence, D. A., Weigle, W. O., and Spiegelberg, H. L., 1975, Immunoglobulins cytophiic for human lymphocytes, monocytes, and neutrophils, J. Clin. Invest. 55:368–376.
Low, T. L. K., Liu, Y.-S. V., and Putnam, F. W., 1976, Structure, function, and evolutionary relationships of Fc domains of human immunoglobulins A, G, M, and E, Science 191:390–392.
Mackenzie, M. R., Wamer, N. L., Linscott, W. D., and Fudenberg, H. H., 1969, Differentiation of human IgM subclasses by the ability to interact with a factor resembling the first component of complement, J. Immunol. 103:607–612.
MacLennan, I. C. M., Connell, G. E., and Gotch, F. M., 1974, Effector activating determinants on IgG. Il. Differentiation of the combining sites for Clq from those for cytotoxic K-cells and neutrophils by plasmin digestion of rabbit IgG, Immunology 26:303–310.
Matre, R., Tonder, O., and Endresen, C., 1975, Fc receptors in human placenta, Scand. J. Immunol. 4:741–745.
McNabb, T., Koh, T. Y., Dorrington, K. J., and Painter, R. H., 1976, Structure and function of immunoglobulin domains. V. Binding of immunoglobulin G and fragments to placental membrane preparations, J. Immunol. 117:882–888.
Messner, R. P., and Jelinek, J., 1970, Receptors for human yG globulin on human neutrophils, J. Clin. Invest. 49:2165–2171.
Metzger, H., 1974, Effect of antigen binding on the properties of antibody, Adv. Immunol. 18:169–207.
Michaelsen, T. E., Wisloff, F., and Natvig, J. B., 1975, Structural requirements in the Fc region of rabbit IgG antibodies necessary to induce cytotoxicity by human lymphocytes, Scand. J. Imnumol 4:71.
Michaelsen, T. E., Frangione, B., and Franklin, E. C., 1977, Primary structure of the “hinge” region of human IgG3: Probable quadruplication of a 15-amino acid residue basic unit, J. Biol. Chem. 252:883–889
Minta, J. O., and Painter, R. H., 1972, A re-examination of the ability of pFc’ and Fe’ to participate in passive cutaneous anaphylaxis, Immunochemistry 9:1041–1048.
Müller-Eberhard, H. J., 1974, Patterns of complement activation, Prog. Immunol. II 1:173–182.
Müller-Eberhard, H. J., 1975, Complement, Annu. Rev. Biochem. 44:697–724.
Okafor, G. O., Turner, M. W., and Hay, F. C., 1974, Localization of monocyte binding site of human immunoglobulin G, Nature (London) 248:228–230.
Ovary, Z., 1964, Passive cutaneous anaphylaxis, in: Immunological Methods (J. F. Ackroyd, ed.), p. 259, Blackwell, London.
Ovary, Z., Salsuk, P. H., Quijada, L., and Lamm, M. E., 1976, Biologic activities of rabbit immunoglobulin G in relation to domains of the Fc region, J. Immunol. 116:1265–1271.
Painter, R. H., Yasmeen, D., Assimeh, S. N., and Poulik, M. D., 1974, Complement fixing and macrophage opsonizing activities associated with ßp microglobulin, Immunol. Commun. 3:19–34.
Philips-Quagliata, J. M., Levine, B. B., Quagliata, F., and Uhr, J. W., 1971, Mechanisms underlying binding of immune complexes to macrophages, J. Exp. Med. 133:589–601.
Porter, R. R., 1959, The hydrolysis of rabbit y-globulin and antibodies with crystalline papain, Biochem. J. 73:119–126.
Prahl, J. W., 1967, Enzymic degradation of the Fc fragment of rabbit immunoglobulin IgG, Biochem. J. 104:647–655.
Prystowsky, M. B., Erickson, B. W., and Kehoe, J. M., 1977, Interaction of synthetic peptides from the CH2 domain of immunoglobulin G with the Clq component of serum complement, Fed. Proc. Fed. Am. Soc. Exp. Biol. 36:1310.
Putnam, F. W., Florent, G. Paul, C. Shinoda, T., and Shimizu, A., 1973, Complete amino acid sequence of the mu heavy chain of a human IgM immunoglobulin, Science 182:287–291.
Ramasamy, R., Secher, D. S., and Adetugbo, K., 1975, CH3 domain of IgG as binding site to Fc receptor on mouse lymphocytes, Nature (London) 253:656.
Rhodes, J., 1973, Receptor for monomeric IgM on guinea pig splenic macrophages, Nature (London) 243:527–528.
Schlessinger, J., Steinberg, I. Z., Givol, D., Hochman, J., and Pecht, I., 1975, Antigen induced conformational changes in antibodies and their Fab fragments studied by circular polarization of fluorescence, Proc. Natl. Acad. Sci. U.S.A. 72:2775–2779.
Schumaker, V. N., Calcott, M. A., Spiegelberg, H. L., and Müller-Eberhard, H. J., 1976, Ultracentrifuge studies of the binding of IgG of different subclasses to the Clq subunit of the first component of complement, Biochemistry 15:5175–5181.
Sjödahl, J., 1976, Repetitive sequences in protein A from Staphylococcus aureus: Three highly homologous Fc-binding regions, FEES Lett. 67:62–67.
Sjoquist, J., Meloun, B., and Hjelm, H., 1972, Protein A isolated from Staphylococcus aureus after digestion with lysostaphin, Eur. J. Biochem. 29:572–578.
Spiegelberg, H. L., and Fishkin, B. C., 1972, The catabolism of human yG immunoglobulins of different heavy chain subclasses. III. The catabolism of heavy chain disease proteins and of Fc fragments of myeloma proteins, Clin. Exp. Immunol. 10:599–607.
Stewart, G. A., Smith, A. K., and Stanworth, D. R., 1973, Biological activities associated with the Facb fragment of rabbit IgG, Immunochemistry 10:755–760.
Stout, R. D., and Herzenberg, L. A., 1975, The Fc receptor on thymus-derived lymphocytes, J. Exp. Med. 142:611–621.
Strober, W., Wochner, R. D., Barlow, M. H., McFarlin, D. E., and Waldman, T. A., 1968, Immunoglobulin metabolism in ataxia telangiectasia, J. Clin. Invest. 47:1905–1915.
Sullivan, A. L., Grimley, P. M., and Metzger, H., 1971, Electron microscopic localization of immunoglobulin E on the surface membrane of human basophils, J. Exp. Med. 134:1403–1416.
Takatsu, K., Ishizaka, T., and Ishizaka, K., 1975, Biological significance of disulfide bonds in human IgE molecules, J. Immunol. 114:1838–1845.
Utsumi, S., 1969, Stepwise cleavage of rabbit immunoglobulin G by papain and isolation of four types of biologically active Fc fragments, Biochem. J. 112:343–355.
Waldmann, T. A., Strober, W., and Blaese, R. M., 1971, Metabolism of immunoglobulins, in: Progress in Immunology I (B. Amos, ed.), pp. 891–903, Academic Press, New York.
Watanabe, S., Barnikol, H. U., Horn, J., Bertram, J., and Hilschmann, N., 1973, Die Primärstruktur eines monoklonalen IgM-Immunoglobulins (Makroglobulin Gal), KK: Die Aminosäuresequenz der H-kette (ATyp, Subgruppe III), Struktur des gesamten IgM-Moleküls, Hoppe-Seyler’s Z. Physiol. Chem. 354:1505–1509.
Williams, R. C., Griffiths, R. W., Emmons, J. D., and Field, R. C., 1972, Naturally occurring human anti-globulins with specificity for yE, J. Clin. Invest. 51:955–963.
Wisloff, F., Michaelsen, T. E., and Froland, S. S., 1974, Inhibition of antibody-dependent human lymphocyte mediated cytotoxicity by immunoglobulin classes, IgG subclasses, and IgG fragments, Scand. J. Immunol. 3:29–35.
Yasmeen, D., Ellerson, J. R., Dorrington, K. J., and Painter, R. H., 1973, Evidence for the domain hypothesis: Location of the site of cytophilic activity toward guinea pig macrophages in the CH3 homology region of human immunoglobulin G, J. Immunol. 110:1706–1709.
Yasmeen, D., Ellerson, J. R., Dorrington, K. J., and Painter, R. H., 1976, The structure and function of immunoglobulin domains. 4. The distribution of some effector functions among the Cy2 and Cy3 homology regions of human immunoglobulin G, J. Immunol. 116:518–526.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1978 Plenum Publishing Corporation
About this chapter
Cite this chapter
Kehoe, J.M. (1978). The Structural Basis for the Biological Properties of Immunoglobulins. In: Litman, G.W., Good, R.A. (eds) Immunoglobulins. Comprehensive Immunology, vol 5. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-0805-8_6
Download citation
DOI: https://doi.org/10.1007/978-1-4684-0805-8_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-0807-2
Online ISBN: 978-1-4684-0805-8
eBook Packages: Springer Book Archive